Towards measurement of the time-resolved heat release of protein conformation dynamics

Jason Puchalla; Daniel Adamek; Robert Austin

doi:10.1016/j.chemphys.2004.09.006

Towards measurement of the time-resolved heat release of protein conformation dynamics

Jason Puchalla, Daniel Adamek, Robert Austin

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1 Scopus citations

Abstract

We present a way to observe time-resolved heat release using a laminar flow diffusional mixer coupled with a highly sensitive infrared camera which measures the temperature change of the solvent. There are significant benefits to the use of laminar flow mixers for time-resolved calorimetry: (1) The thermal signal can be made position and time-stationary to allow for signal integration; (2) Extremely small volumes (nl/s) of sample are required for a measurement; (3) The same mixing environment can be observed spectroscopically to obtain state occupation information; (4) The mixer allows one to do out of equilibrium dynamic studies. The hope is that these measurements will allow us probe the non-equilibrium thermodynamics as a protein moves along a free energy trajectory from one state to another.

Original language	English (US)
Pages (from-to)	285-290
Number of pages	6
Journal	Chemical Physics
Volume	307
Issue number	2-3 SPEC.ISS.
DOIs	https://doi.org/10.1016/j.chemphys.2004.09.006
State	Published - Dec 27 2004

All Science Journal Classification (ASJC) codes

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1016/j.chemphys.2004.09.006

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title = "Towards measurement of the time-resolved heat release of protein conformation dynamics",

abstract = "We present a way to observe time-resolved heat release using a laminar flow diffusional mixer coupled with a highly sensitive infrared camera which measures the temperature change of the solvent. There are significant benefits to the use of laminar flow mixers for time-resolved calorimetry: (1) The thermal signal can be made position and time-stationary to allow for signal integration; (2) Extremely small volumes (nl/s) of sample are required for a measurement; (3) The same mixing environment can be observed spectroscopically to obtain state occupation information; (4) The mixer allows one to do out of equilibrium dynamic studies. The hope is that these measurements will allow us probe the non-equilibrium thermodynamics as a protein moves along a free energy trajectory from one state to another.",

author = "Jason Puchalla and Daniel Adamek and Robert Austin",

note = "Funding Information: This work was supported by Grants from DARPA (MDA972-00-1-0031), NIH (HG01506), NSF Nanobiology Technology Center (BSCECS9876771) and the State of New Jersey (NJCST 99-100-082-2042-007). Puchalla was supported by a Lewis-Thomas/Bristol Myers Squibb Fellowship. Hays S. Rye of the Department of Molecular Biology, Princeton University provided the GroEL/ES samples, and Daniel Adamek of NASA Huntsville Alabama generously provided access to the FLIR Systems camera. We thank Peter Galajda for fabrication of the through-wafer etched structure. We acknowledge support from the Cornell University National Fabrication Center, where the deep silicon etching process of the device reported here was performed.",

year = "2004",

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day = "27",

doi = "10.1016/j.chemphys.2004.09.006",

language = "English (US)",

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pages = "285--290",

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T1 - Towards measurement of the time-resolved heat release of protein conformation dynamics

AU - Puchalla, Jason

AU - Adamek, Daniel

AU - Austin, Robert

N1 - Funding Information: This work was supported by Grants from DARPA (MDA972-00-1-0031), NIH (HG01506), NSF Nanobiology Technology Center (BSCECS9876771) and the State of New Jersey (NJCST 99-100-082-2042-007). Puchalla was supported by a Lewis-Thomas/Bristol Myers Squibb Fellowship. Hays S. Rye of the Department of Molecular Biology, Princeton University provided the GroEL/ES samples, and Daniel Adamek of NASA Huntsville Alabama generously provided access to the FLIR Systems camera. We thank Peter Galajda for fabrication of the through-wafer etched structure. We acknowledge support from the Cornell University National Fabrication Center, where the deep silicon etching process of the device reported here was performed.

PY - 2004/12/27

Y1 - 2004/12/27

N2 - We present a way to observe time-resolved heat release using a laminar flow diffusional mixer coupled with a highly sensitive infrared camera which measures the temperature change of the solvent. There are significant benefits to the use of laminar flow mixers for time-resolved calorimetry: (1) The thermal signal can be made position and time-stationary to allow for signal integration; (2) Extremely small volumes (nl/s) of sample are required for a measurement; (3) The same mixing environment can be observed spectroscopically to obtain state occupation information; (4) The mixer allows one to do out of equilibrium dynamic studies. The hope is that these measurements will allow us probe the non-equilibrium thermodynamics as a protein moves along a free energy trajectory from one state to another.

AB - We present a way to observe time-resolved heat release using a laminar flow diffusional mixer coupled with a highly sensitive infrared camera which measures the temperature change of the solvent. There are significant benefits to the use of laminar flow mixers for time-resolved calorimetry: (1) The thermal signal can be made position and time-stationary to allow for signal integration; (2) Extremely small volumes (nl/s) of sample are required for a measurement; (3) The same mixing environment can be observed spectroscopically to obtain state occupation information; (4) The mixer allows one to do out of equilibrium dynamic studies. The hope is that these measurements will allow us probe the non-equilibrium thermodynamics as a protein moves along a free energy trajectory from one state to another.

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JO - Chemical Physics

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Towards measurement of the time-resolved heat release of protein conformation dynamics

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